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P16615

- AT2A2_HUMAN

UniProt

P16615 - AT2A2_HUMAN

Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Gene

ATP2A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle.1 Publication

    Catalytic activityi

    ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

    Enzyme regulationi

    Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi304 – 3041Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi305 – 3051Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi307 – 3071Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi309 – 3091Calcium 2By similarity
    Active sitei351 – 35114-aspartylphosphate intermediateBy similarity
    Metal bindingi702 – 7021MagnesiumBy similarity
    Metal bindingi706 – 7061MagnesiumBy similarity
    Metal bindingi767 – 7671Calcium 1By similarity
    Metal bindingi770 – 7701Calcium 1By similarity
    Metal bindingi795 – 7951Calcium 2By similarity
    Metal bindingi798 – 7981Calcium 1By similarity
    Metal bindingi799 – 7991Calcium 1By similarity
    Metal bindingi799 – 7991Calcium 2By similarity
    Metal bindingi907 – 9071Calcium 1By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium-transporting ATPase activity Source: ProtInc
    3. calcium-transporting ATPase activity involved in regulation of cardiac muscle cell membrane potential Source: BHF-UCL
    4. enzyme binding Source: BHF-UCL
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: IntAct
    7. protein C-terminus binding Source: UniProtKB
    8. S100 protein binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. calcium ion transmembrane transport Source: GOC
    3. cell adhesion Source: ProtInc
    4. cellular calcium ion homeostasis Source: BHF-UCL
    5. epidermis development Source: ProtInc
    6. ER-nucleus signaling pathway Source: Ensembl
    7. ion transmembrane transport Source: Reactome
    8. negative regulation of heart contraction Source: Ensembl
    9. positive regulation of heart rate Source: BHF-UCL
    10. regulation of cardiac muscle cell membrane potential Source: BHF-UCL
    11. regulation of the force of heart contraction Source: Ensembl
    12. relaxation of cardiac muscle Source: BHF-UCL
    13. sarcoplasmic reticulum calcium ion transport Source: BHF-UCL
    14. transmembrane transport Source: Reactome
    15. transport Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_118798. Pre-NOTCH Processing in Golgi.
    REACT_23765. Reduction of cytosolic Ca++ levels.
    REACT_25149. Ion transport by P-type ATPases.
    SignaLinkiP16615.

    Protein family/group databases

    TCDBi3.A.3.2.7. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (EC:3.6.3.8)
    Short name:
    SERCA2
    Short name:
    SR Ca(2+)-ATPase 2
    Alternative name(s):
    Calcium pump 2
    Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
    Endoplasmic reticulum class 1/2 Ca(2+) ATPase
    Gene namesi
    Name:ATP2A2
    Synonyms:ATP2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:812. ATP2A2.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB
    2. integral component of plasma membrane Source: ProtInc
    3. intracellular membrane-bounded organelle Source: ProtInc
    4. membrane Source: MGI
    5. platelet dense tubular network membrane Source: Reactome
    6. sarcoplasmic reticulum Source: UniProtKB
    7. sarcoplasmic reticulum membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Acrokeratosis verruciformis (AKV) [MIM:101900]: A localized disorder of keratinization, which is inherited as an autosomal dominant trait. Its onset is early in life with multiple flat-topped, flesh-colored papules on the hands and feet, punctate keratoses on the palms and soles, with varying degrees of nail involvement. The histopathology shows a distinctive pattern of epidermal features with hyperkeratosis, hypergranulosis and acanthosis together with papillomatosis. These changes are frequently associated with circumscribed elevations of the epidermis that are said to resemble church spires. There are no features of dyskeratosis or acantholysis, the typical findings in lesions of Darier disease.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti602 – 6021P → L in AKV; loss of activity. 1 Publication
    VAR_017532
    Darier disease (DD) [MIM:124200]: A skin disorder characterized by warty papules and plaques in seborrheic areas (central trunk, flexures, scalp and forehead), palmoplantar pits and distinctive nail abnormalities. It is due to loss of adhesion between epidermal cells (acantholysis) and abnormal keratinization. Patients with mild disease may have no more than a few scattered keratotic papules or subtle nail changes, whereas those with severe disease are handicapped by widespread malodorous keratotic plaques. Some patients present with hemorrhage into acantholytic vesicles on the palms and dorsal aspects of the fingers which gives rise to black macules. In a few families affected by Darier disease, neuropsychiatric abnormalities such as mild mental retardation, schizophrenia, bipolar disorder and epilepsy have been reported. Stress, UV exposure, heat, sweat, friction and oral contraception exacerbate disease symptoms. Clinical variants of Darier disease include hypertrophic, vesicobullous, hypopigmented, cornifying, zosteriform or linear, acute and comedonal subtypes. Comedonal Darier disease is characterized by the coexistence of acne-like comedonal lesions with typical Darier hyperkeratotic papules on light-exposed areas. At histopathologic level, comedonal Darier disease differs from classic Darier disease in the prominent follicular involvement and the presence of greatly elongated dermal villi.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231G → E in DD. 1 Publication
    Corresponds to variant rs28929478 [ dbSNP | Ensembl ].
    VAR_008608
    Natural varianti39 – 391N → T in DD. 1 Publication
    VAR_008609
    Natural varianti41 – 411Missing in DD; comedonal type. 1 Publication
    VAR_063398
    Natural varianti47 – 471K → KMFLTGK in DD.
    VAR_008610
    Natural varianti65 – 651L → S in DD; severe form.
    VAR_008611
    Natural varianti131 – 1311R → Q in DD.
    VAR_008612
    Natural varianti160 – 1601P → L in DD.
    VAR_008613
    Natural varianti186 – 1861S → P in DD.
    VAR_008614
    Natural varianti211 – 2111G → D in DD; severe form.
    VAR_008615
    Natural varianti223 – 2231V → M in DD.
    VAR_008616
    Natural varianti268 – 2681C → F in DD; haemorrhagic lesions.
    VAR_008617
    Natural varianti310 – 3101G → V in DD.
    VAR_008618
    Natural varianti318 – 3181C → R in DD; severe form.
    VAR_008619
    Natural varianti348 – 3481I → T in DD.
    VAR_008620
    Natural varianti357 – 3571T → K in DD. 1 Publication
    VAR_009508
    Natural varianti412 – 4121E → G in DD.
    VAR_008621
    Natural varianti495 – 4951S → F in DD. 1 Publication
    VAR_008622
    Natural varianti560 – 5601C → R in DD; neuropsychiatric phenotype. 1 Publication
    VAR_008623
    Natural varianti675 – 6751F → S in DD; multiple neuropsychiatric features.
    VAR_008624
    Natural varianti683 – 6831K → E in DD; depression.
    VAR_008625
    Natural varianti702 – 7021D → N in DD; moderate form.
    VAR_008626
    Natural varianti745 – 7451A → D in DD; moderate form.
    VAR_008627
    Natural varianti749 – 7491G → R in DD. 1 Publication
    VAR_009509
    Natural varianti754 – 7541Missing in DD.
    VAR_008628
    Natural varianti765 – 7651S → L in DD. 1 Publication
    VAR_008629
    Natural varianti767 – 7671N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype.
    VAR_008630
    Natural varianti769 – 7691G → R in DD.
    VAR_008631
    Natural varianti803 – 8031A → T in DD; mild/moderate form.
    VAR_008632
    Natural varianti838 – 8381A → P in DD; severe form; petit mal epilepsy.
    VAR_008633
    Natural varianti843 – 8431V → F in DD; depression.
    VAR_008634
    Natural varianti875 – 8751C → G in DD; retinitis pigmentosa.
    VAR_008635
    Natural varianti920 – 9201S → Y in DD; mild/moderate/severe form; one patient with epilepsy.
    VAR_008636
    Natural varianti943 – 9431H → R in DD; learning difficulties.
    VAR_008637
    Natural varianti975 – 9751P → R in DD.
    VAR_008638

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    MIMi101900. phenotype.
    124200. phenotype.
    Orphaneti79151. Acrokeratosis verruciformis of Hopf.
    218. Darier disease.
    PharmGKBiPA71.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10421042Sarcoplasmic/endoplasmic reticulum calcium ATPase 2PRO_0000046196Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki143 – 143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei294 – 2941Nitrated tyrosine1 Publication
    Modified residuei295 – 2951Nitrated tyrosine1 Publication
    Modified residuei663 – 6631Phosphoserine3 Publications

    Post-translational modificationi

    Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.1 Publication

    Keywords - PTMi

    Isopeptide bond, Nitration, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP16615.
    PaxDbiP16615.
    PRIDEiP16615.

    PTM databases

    PhosphoSiteiP16615.

    Expressioni

    Tissue specificityi

    Isoform 1 is widely expressed in smooth muscle and nonmuscle tissues such as in adult skin epidermis, with highest expression in liver, pancreas and lung, and intermediate expression in brain, kidney and placenta. Also expressed at lower levels in heart and skeletal muscle. Isoforms 2 and 3 are highly expressed in the heart and slow twitch skeletal muscle. Expression of isoform 3 is predominantly restricted to cardiomyocytes and in close proximity to the sarcolemma. Both isoforms are mildly expressed in lung, kidney, liver, pancreas and placenta. Expression of isoform 3 is amplified during monocytic differentiation and also observed in the fetal heart.3 Publications

    Gene expression databases

    ArrayExpressiP16615.
    BgeeiP16615.
    CleanExiHS_ATP2A2.
    GenevestigatoriP16615.

    Organism-specific databases

    HPAiHPA062605.

    Interactioni

    Subunit structurei

    Associated with phospholamban (PLN) By similarity. Isoform 1 interacts with TRAM2 (via C-terminus). Interacts with HAX1. Interacts with S100A8 and S100A9 By similarity. Interacts with SLC35G1 and STIM1.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    OPRD1P411433EBI-358933,EBI-2624456

    Protein-protein interaction databases

    BioGridi106978. 39 interactions.
    IntActiP16615. 19 interactions.
    MINTiMINT-4991144.
    STRINGi9606.ENSP00000324892.

    Structurei

    3D structure databases

    ProteinModelPortaliP16615.
    SMRiP16615. Positions 1-992.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4848CytoplasmicBy similarityAdd
    BLAST
    Topological domaini70 – 8920LumenalBy similarityAdd
    BLAST
    Topological domaini111 – 253143CytoplasmicBy similarityAdd
    BLAST
    Topological domaini274 – 29522LumenalBy similarityAdd
    BLAST
    Topological domaini314 – 756443CytoplasmicBy similarityAdd
    BLAST
    Topological domaini777 – 78610LumenalBy similarity
    Topological domaini808 – 82720CytoplasmicBy similarityAdd
    BLAST
    Topological domaini851 – 89646LumenalBy similarityAdd
    BLAST
    Topological domaini917 – 92913CytoplasmicBy similarityAdd
    BLAST
    Topological domaini949 – 96315LumenalBy similarityAdd
    BLAST
    Topological domaini985 – 104258CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei49 – 6921Helical; Name=1By similarityAdd
    BLAST
    Transmembranei90 – 11021Helical; Name=2By similarityAdd
    BLAST
    Transmembranei254 – 27320Helical; Name=3By similarityAdd
    BLAST
    Transmembranei296 – 31318Helical; Name=4By similarityAdd
    BLAST
    Transmembranei757 – 77620Helical; Name=5By similarityAdd
    BLAST
    Transmembranei787 – 80721Helical; Name=6By similarityAdd
    BLAST
    Transmembranei828 – 85023Helical; Name=7By similarityAdd
    BLAST
    Transmembranei897 – 91620Helical; Name=8By similarityAdd
    BLAST
    Transmembranei930 – 94819Helical; Name=9By similarityAdd
    BLAST
    Transmembranei964 – 98421Helical; Name=10By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni370 – 40031Interacts with phospholamban 1By similarityAdd
    BLAST
    Regioni575 – 59420Interacts with HAX1Add
    BLAST
    Regioni787 – 80721Interacts with phospholamban 2By similarityAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOGENOMiHOG000265621.
    HOVERGENiHBG105648.
    InParanoidiP16615.
    KOiK05853.
    OMAiRVEGDTC.
    OrthoDBiEOG73Z2SF.
    PhylomeDBiP16615.
    TreeFamiTF300651.

    Family and domain databases

    Gene3Di1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProiIPR005782. ATPase_P-typ_Ca-transp_IIA.
    IPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view]
    PfamiPF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    PR00120. HATPASE.
    SMARTiSM00831. Cation_ATPase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: SERCA2 transcripts differ only in their 3'-UTR region and are expressed in a tissue-specific manner.

    Isoform 1 (identifier: P16615-1) [UniParc]FASTAAdd to Basket

    Also known as: ATP2A2B, Class 2-4, HK1, SERCA2b

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL     50
    ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA 100
    NAIVGVWQER NAENAIEALK EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI 150
    VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV 200
    NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV ATEQERTPLQ 250
    QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV 300
    ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS 350
    DKTGTLTTNQ MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK 400
    PVNCHQYDGL VELATICALC NDSALDYNEA KGVYEKVGEA TETALTCLVE 450
    KMNVFDTELK GLSKIERANA CNSVIKQLMK KEFTLEFSRD RKSMSVYCTP 500
    NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV KQKIMSVIRE 550
    WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD 600
    PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK 650
    AFTGREFDEL NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT 700
    GDGVNDAPAL KKAEIGIAMG SGTAVAKTAS EMVLADDNFS TIVAAVEEGR 750
    AIYNNMKQFI RYLISSNVGE VVCIFLTAAL GFPEALIPVQ LLWVNLVTDG 800
    LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG CYVGAATVGA 850
    AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL 900
    SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE 950
    PLPLIFQITP LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP 1000
    ATKSCSFSAC TDGISWPFVL LIMPLVIWVY STDTNFSDMF WS 1042

    Note: Ubiquitous housekeeping isoform.

    Length:1,042
    Mass (Da):114,757
    Last modified:August 1, 1990 - v1
    Checksum:i5462FF2DA7FB630A
    GO
    Isoform 2 (identifier: P16615-2) [UniParc]FASTAAdd to Basket

    Also known as: ATP2A2A, Class 1, HK2, SERCA2a

    The sequence of this isoform differs from the canonical sequence as follows:
         994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE

    Note: Cardiac/slow twitch, muscle specific isoform. Has a lower affinity for calcium and a higher catalytic turnover rate.

    Show »
    Length:997
    Mass (Da):109,691
    Checksum:iDD57D12A2B24FEC1
    GO
    Isoform 3 (identifier: P16615-3) [UniParc]FASTAAdd to Basket

    Also known as: SERCA2C

    The sequence of this isoform differs from the canonical sequence as follows:
         994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → VLSSEL

    Note: May be due to intron retention. Shows a lower apparent affinity for cytosolic calcium than isoform 2 and a catalytic turnover rate similar to isoform 1.

    Show »
    Length:999
    Mass (Da):109,893
    Checksum:iF6BE03E546453B24
    GO
    Isoform 4 (identifier: P16615-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         155-181: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,015
    Mass (Da):111,847
    Checksum:i6C99B5C382834A63
    GO
    Isoform 5 (identifier: P16615-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → DIIK

    Note: No experimental confirmation available.

    Show »
    Length:997
    Mass (Da):109,734
    Checksum:iD570A12D5B24FEC1
    GO

    Sequence cautioni

    The sequence BAG57266.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231G → E in DD. 1 Publication
    Corresponds to variant rs28929478 [ dbSNP | Ensembl ].
    VAR_008608
    Natural varianti39 – 391N → T in DD. 1 Publication
    VAR_008609
    Natural varianti41 – 411Missing in DD; comedonal type. 1 Publication
    VAR_063398
    Natural varianti47 – 471K → KMFLTGK in DD.
    VAR_008610
    Natural varianti65 – 651L → S in DD; severe form.
    VAR_008611
    Natural varianti131 – 1311R → Q in DD.
    VAR_008612
    Natural varianti160 – 1601P → L in DD.
    VAR_008613
    Natural varianti186 – 1861S → P in DD.
    VAR_008614
    Natural varianti211 – 2111G → D in DD; severe form.
    VAR_008615
    Natural varianti223 – 2231V → M in DD.
    VAR_008616
    Natural varianti268 – 2681C → F in DD; haemorrhagic lesions.
    VAR_008617
    Natural varianti310 – 3101G → V in DD.
    VAR_008618
    Natural varianti318 – 3181C → R in DD; severe form.
    VAR_008619
    Natural varianti348 – 3481I → T in DD.
    VAR_008620
    Natural varianti357 – 3571T → K in DD. 1 Publication
    VAR_009508
    Natural varianti412 – 4121E → G in DD.
    VAR_008621
    Natural varianti495 – 4951S → F in DD. 1 Publication
    VAR_008622
    Natural varianti560 – 5601C → R in DD; neuropsychiatric phenotype. 1 Publication
    VAR_008623
    Natural varianti602 – 6021P → L in AKV; loss of activity. 1 Publication
    VAR_017532
    Natural varianti675 – 6751F → S in DD; multiple neuropsychiatric features.
    VAR_008624
    Natural varianti683 – 6831K → E in DD; depression.
    VAR_008625
    Natural varianti702 – 7021D → N in DD; moderate form.
    VAR_008626
    Natural varianti745 – 7451A → D in DD; moderate form.
    VAR_008627
    Natural varianti749 – 7491G → R in DD. 1 Publication
    VAR_009509
    Natural varianti754 – 7541Missing in DD.
    VAR_008628
    Natural varianti765 – 7651S → L in DD. 1 Publication
    VAR_008629
    Natural varianti767 – 7671N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype.
    VAR_008630
    Natural varianti769 – 7691G → R in DD.
    VAR_008631
    Natural varianti803 – 8031A → T in DD; mild/moderate form.
    VAR_008632
    Natural varianti838 – 8381A → P in DD; severe form; petit mal epilepsy.
    VAR_008633
    Natural varianti843 – 8431V → F in DD; depression.
    VAR_008634
    Natural varianti875 – 8751C → G in DD; retinitis pigmentosa.
    VAR_008635
    Natural varianti920 – 9201S → Y in DD; mild/moderate/severe form; one patient with epilepsy.
    VAR_008636
    Natural varianti943 – 9431H → R in DD; learning difficulties.
    VAR_008637
    Natural varianti975 – 9751P → R in DD.
    VAR_008638

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei155 – 18127Missing in isoform 4. 1 PublicationVSP_039392Add
    BLAST
    Alternative sequencei994 – 104249GKECV…DMFWS → AILE in isoform 2. 1 PublicationVSP_000358Add
    BLAST
    Alternative sequencei994 – 104249GKECV…DMFWS → VLSSEL in isoform 3. 1 PublicationVSP_039393Add
    BLAST
    Alternative sequencei994 – 104249GKECV…DMFWS → DIIK in isoform 5. CuratedVSP_039394Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23114 mRNA. Translation: AAA53193.1.
    M23116 Genomic DNA. Translation: AAA52757.1.
    M23115 mRNA. Translation: AAA53194.1.
    M23278, M23116 Genomic DNA. Translation: AAA52758.1.
    AC006088 Genomic DNA. No translation available.
    BC035588 mRNA. Translation: AAH35588.1.
    AK293877 mRNA. Translation: BAG57266.1. Different initiation.
    AY186578 mRNA. Translation: AAO47398.1.
    CCDSiCCDS9143.1. [P16615-2]
    CCDS9144.1. [P16615-1]
    PIRiA31981.
    B31981.
    RefSeqiNP_001672.1. NM_001681.3. [P16615-2]
    NP_733765.1. NM_170665.3. [P16615-1]
    XP_005253945.1. XM_005253888.1. [P16615-3]
    UniGeneiHs.506759.

    Genome annotation databases

    EnsembliENST00000308664; ENSP00000311186; ENSG00000174437. [P16615-2]
    ENST00000539276; ENSP00000440045; ENSG00000174437. [P16615-1]
    ENST00000553144; ENSP00000450407; ENSG00000174437.
    GeneIDi488.
    KEGGihsa:488.
    UCSCiuc001tqk.4. human. [P16615-1]
    uc001tql.4. human. [P16615-2]

    Polymorphism databases

    DMDMi114312.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23114 mRNA. Translation: AAA53193.1 .
    M23116 Genomic DNA. Translation: AAA52757.1 .
    M23115 mRNA. Translation: AAA53194.1 .
    M23278 , M23116 Genomic DNA. Translation: AAA52758.1 .
    AC006088 Genomic DNA. No translation available.
    BC035588 mRNA. Translation: AAH35588.1 .
    AK293877 mRNA. Translation: BAG57266.1 . Different initiation.
    AY186578 mRNA. Translation: AAO47398.1 .
    CCDSi CCDS9143.1. [P16615-2 ]
    CCDS9144.1. [P16615-1 ]
    PIRi A31981.
    B31981.
    RefSeqi NP_001672.1. NM_001681.3. [P16615-2 ]
    NP_733765.1. NM_170665.3. [P16615-1 ]
    XP_005253945.1. XM_005253888.1. [P16615-3 ]
    UniGenei Hs.506759.

    3D structure databases

    ProteinModelPortali P16615.
    SMRi P16615. Positions 1-992.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106978. 39 interactions.
    IntActi P16615. 19 interactions.
    MINTi MINT-4991144.
    STRINGi 9606.ENSP00000324892.

    Chemistry

    BindingDBi P16615.
    ChEMBLi CHEMBL3901.

    Protein family/group databases

    TCDBi 3.A.3.2.7. the p-type atpase (p-atpase) superfamily.

    PTM databases

    PhosphoSitei P16615.

    Polymorphism databases

    DMDMi 114312.

    Proteomic databases

    MaxQBi P16615.
    PaxDbi P16615.
    PRIDEi P16615.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308664 ; ENSP00000311186 ; ENSG00000174437 . [P16615-2 ]
    ENST00000539276 ; ENSP00000440045 ; ENSG00000174437 . [P16615-1 ]
    ENST00000553144 ; ENSP00000450407 ; ENSG00000174437 .
    GeneIDi 488.
    KEGGi hsa:488.
    UCSCi uc001tqk.4. human. [P16615-1 ]
    uc001tql.4. human. [P16615-2 ]

    Organism-specific databases

    CTDi 488.
    GeneCardsi GC12P110719.
    HGNCi HGNC:812. ATP2A2.
    HPAi HPA062605.
    MIMi 101900. phenotype.
    108740. gene.
    124200. phenotype.
    neXtProti NX_P16615.
    Orphaneti 79151. Acrokeratosis verruciformis of Hopf.
    218. Darier disease.
    PharmGKBi PA71.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0474.
    HOGENOMi HOG000265621.
    HOVERGENi HBG105648.
    InParanoidi P16615.
    KOi K05853.
    OMAi RVEGDTC.
    OrthoDBi EOG73Z2SF.
    PhylomeDBi P16615.
    TreeFami TF300651.

    Enzyme and pathway databases

    Reactomei REACT_118798. Pre-NOTCH Processing in Golgi.
    REACT_23765. Reduction of cytosolic Ca++ levels.
    REACT_25149. Ion transport by P-type ATPases.
    SignaLinki P16615.

    Miscellaneous databases

    ChiTaRSi ATP2A2. human.
    GenomeRNAii 488.
    NextBioi 2031.
    PROi P16615.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16615.
    Bgeei P16615.
    CleanExi HS_ATP2A2.
    Genevestigatori P16615.

    Family and domain databases

    Gene3Di 1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProi IPR005782. ATPase_P-typ_Ca-transp_IIA.
    IPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view ]
    Pfami PF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    PR00120. HATPASE.
    SMARTi SM00831. Cation_ATPase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01116. ATPase-IIA1_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of cDNAs from human kidney coding for two alternatively spliced products of the cardiac Ca2+-ATPase gene."
      Lytton J., Maclennan D.H.
      J. Biol. Chem. 263:15024-15031(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
      Tissue: Kidney.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Eye.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-1042 (ISOFORM 4).
      Tissue: Cerebellum.
    5. "Identification of a new SERCA2 splice variant regulated during monocytic differentiation."
      Gelebart P., Martin V., Enouf J., Papp B.
      Biochem. Biophys. Res. Commun. 303:676-684(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 954-1042 (ISOFORM 3), TISSUE SPECIFICITY.
    6. "TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis."
      Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.
      Mol. Cell. Biol. 24:1758-1768(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAM2.
    7. "Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging."
      Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.
      Am. J. Physiol. 290:H2220-H2227(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NITRATION AT TYR-294 AND TYR-295.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival."
      Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D., Kontrogianni-Konstantopoulos A., Kranias E.G.
      Mol. Biol. Cell 20:306-318(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HAX1.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters."
      Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.
      Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC35G1 AND STIM1.
    15. "Spectrum of novel ATP2A2 mutations in patients with Darier's disease."
      Sakuntabhai A., Burge S., Monk S., Hovnanian A.
      Hum. Mol. Genet. 8:1611-1619(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DD.
    16. "ATP2A2 mutations in Darier's disease: variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class."
      Ruiz-Perez V.L., Carter S.A., Healy E., Todd C., Rees J.L., Steijlen P.M., Carmichael A.J., Lewis H.M., Hohl D., Itin P., Vahlquist A., Gobello T., Mazzanti C., Reggazini R., Nagy G., Munro C.S., Strachan T.
      Hum. Mol. Genet. 8:1621-1630(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DD, TISSUE SPECIFICITY.
    17. "ATP2A2 mutations in Darier's disease and their relationship to neuropsychiatric phenotypes."
      Jacobsen N.J.O., Lyons I., Hoogendoorn B., Burge S., Kwok P.-Y., O'Donovan M.C., Craddock N., Owen M.J.
      Hum. Mol. Genet. 8:1631-1636(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DD THR-39; ARG-560 AND LEU-765.
    18. Cited for: VARIANTS DD GLU-23; LYS-357; PHE-495 AND ARG-749.
    19. "Acrokeratosis verruciformis of Hopf is caused by mutation in ATP2A2: evidence that it is allelic to Darier's disease."
      Dhitavat J., Macfarlane S., Dode L., Leslie N., Sakuntabhai A., MacSween R., Saihan E., Hovnanian A.
      J. Invest. Dermatol. 120:229-232(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AKV LEU-602.
    20. "Ca2+-ATPases in non-failing and failing heart: evidence for a novel cardiac sarco/endoplasmic reticulum Ca2+-ATPase 2 isoform (SERCA2c)."
      Dally S., Bredoux R., Corvazier E., Andersen J.P., Clausen J.D., Dode L., Fanchaouy M., Gelebart P., Monceau V., Del Monte F., Gwathmey J.K., Hajjar R., Chaabane C., Bobe R., Raies A., Enouf J.
      Biochem. J. 395:249-258(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    21. "Three-base deletion mutation c.120_122delGTT in ATP2A2 leads to the unique phenotype of comedonal Darier disease."
      Tsuruta D., Akiyama M., Ishida-Yamamoto A., Imanishi H., Mizuno N., Sowa J., Kobayashi H., Ishii M., Kurokawa I., Shimizu H.
      Br. J. Dermatol. 162:687-689(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DD LEU-41 DEL.

    Entry informationi

    Entry nameiAT2A2_HUMAN
    AccessioniPrimary (citable) accession number: P16615
    Secondary accession number(s): A6NDN7
    , B4DF05, P16614, Q86VJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 176 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3